Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00038a024
Reference56 articles.
1. The Structure of a Bacterial Ferredoxin
2. Removal of the high-potential iron-sulfur [4Fe-4S] center of the .beta.-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes
3. Site-directed mutagenesis of conserved cysteine residues within the .beta. subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes
4. Fumarate Reductase Mutants of Escherichia coli That Lack Covalently Bound Flavin
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